Yeast phosphofructokinase: Physical parameters, molecular weight and subunit structure
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منابع مشابه
Rabbit muscle phosphofructokinase: studies of the subunit molecular weight and structure. Isolation of carboxymethylated cysteinyl peptides and sedimentation equilibrium studies.
The molecular weight of the subunit of rabbit muscle phosphofructokinase has been investigated by techniques which include sodium dodecyl sulfate gel electrophoresis, sedimentation equilibrium experiments, and the isolation of carboxymethylcysteine-containing tryptic peptides. Sedimentation equilibrium experiments in high concentrations of guanidine, in 0.5 M acetic or propionic acid, yield val...
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Mutant alleles of the gene PFK2 have been obtained that alter the sensitivity to ATP inhibition of the soluble yeast phosphofructokinase. One of the alleles makes the enzyme sensitive to micromolar concentrations of ATP. Intragenic revertants of PFK2 mutants confirm that the PFK2 gene determines not only the regulatory properties of the soluble enzyme but also the catalytic activity of particul...
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The properties and subunit composition of the RNA extracted from RD-114 virions have been studied. The RNA extracted from the virion has a sedimentation coefficient of 52S in a nondenaturing aqueous electrolyte. The estimated molecular weight by sedimentation in nondenaturing and weakly denaturing media is in the range 5.7 X 10(6) to 7.0 X 10(6). By electron microscopy, under moderately denatur...
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Mutants of Saccharomyces cerevisiae completely lacking the soluble glycolytic enzyme fructose-6-P kinase are described. The mutations are semidominant, do not complement one another, and define a gene PFKl located 28-cm distal to rnal on the extended right arm of chromosome XIII. Of 10 independent mutants, 3 can be suppressed by ochre suppressors. All mutants examined synthesize proteins that c...
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The alcohol dehydrogenases (ADH) crystallized from yeast (1, 2) and from horse liver (3) differ in many of their properties. The mammalian enzyme forms a complex with reduced diphosphopyridine nucleotide in which the absorption band of the coenzyme at 340 rnp is shifted to 325 rnh (4). This permitted the direct study by Theorell and Chance (5) of the stoichiometry and dissociation constant of t...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1972
ISSN: 0014-5793
DOI: 10.1016/0014-5793(72)80238-2